Hydrogen/deuterium exchange mass spectrometry--a window into amyloid structure.
Hydrogen/deuterium exchange mass spectrometry--a window into amyloid structure.
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DOI：
10.1002/chin.200649279
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发表时间：
2006-09
影响因子：
18.3
通讯作者：
I. Kheterpal;R. Wetzel
中科院分区：
文献类型：
--
作者：
I. Kheterpal;R. Wetzel
淀粉样原纤维的β-折叠网络是这类蛋白质结构的主要结构特征。观察导致纤维和其他聚集体形成的蛋白质错误折叠事件的一个吸引人的方法是考虑天然蛋白质二级结构是如何重新排列以产生聚集结构中的氢键关系的。本文介绍了氢-氚交换质谱学(HX-MS)方法在蛋白质聚集体二级结构研究中的应用。这包括探索单体、原纤维和纤维的结构，这些状态之间的结构关系，氢键对纤维稳定性的能量贡献，以及氢键网络的可塑性。
The beta-sheet network of the amyloid fibril is a dominant structural feature of this class of protein structures. An attractive way to view the protein misfolding events that lead to the formation of fibrils and other aggregates is to consider how native protein secondary structure rearranges to yield the H-bonding relationships within the aggregate structure. We describe here the application of hydrogen-deuterium exchange mass spectrometry (HX-MS) methods to probe the secondary structure of protein aggregates. This includes exploration of the structures of monomers, protofibrils, and fibrils, the structural relationships among these states, the energetic contribution of H-bonding to fibril stability, and the plasticity of the H-bond network.